Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: resonance assignment of native bacteriorhodopsin

M. Schubert, M Kolbe, B. Kessler, D. Oesterhelt, P. Schmieder

Chembiochem (2002) 3, 1019-1023

A solution state NMR study of the native integral membrane protein bacteriorhodopsin is presented. Bacteriorhodopsin was used as a model system for proteins consisting of seven transmembrane helices. Experiments using TROSY-type NMR techniques were applied to uniformly 2H/15N- and 2H/13C/15N-labeled samples solubilized with dodecylmaltoside. The assignment of 81 out of 248 residues, mainly in the loop regions, is given. Subsequently, structural and dynamic information is derived from the data.

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